3ALR
Crystal structure of Nanos
Summary for 3ALR
Entry DOI | 10.2210/pdb3alr/pdb |
Descriptor | Nanos protein, ZINC ION (3 entities in total) |
Functional Keywords | zinc-finger, translational repression, rna, 3'-utr, metal binding protein |
Biological source | Danio rerio (Zebrafish) |
Total number of polymer chains | 4 |
Total formula weight | 47290.79 |
Authors | Hashimoto, H.,Hara, K.,Hishiki, A.,Kawaguchi, S.,Shichijo, N.,Nakamura, K.,Unzai, S.,Tamaru, Y.,Shimizu, T.,Sato, M. (deposition date: 2010-08-06, release date: 2011-02-02, Last modification date: 2024-03-13) |
Primary citation | Hashimoto, H.,Hara, K.,Hishiki, A.,Kawaguchi, S.,Shichijo, N.,Nakamura, K.,Unzai, S.,Tamaru, Y.,Shimizu, T.,Sato, M. Crystal structure of zinc-finger domain of Nanos and its functional implications Embo Rep., 11:848-853, 2010 Cited by PubMed Abstract: Nanos is an RNA-binding protein that is involved in the development and maintenance of germ cells. In combination with Pumilio, Nanos binds to the 3' untranslated region of a messenger RNA and represses its translation. Nanos has two conserved Cys-Cys-His-Cys zinc-finger motifs that are indispensable for its function. In this study, we have determined the crystal structure of the zinc-finger domain of zebrafish Nanos, for the first time revealing that Nanos adopts a novel zinc-finger structure. In addition, Nanos has a conserved basic surface that is directly involved in RNA binding. Our results provide the structural basis for further studies to clarify Nanos function. PubMed: 20948543DOI: 10.1038/embor.2010.155 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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